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Gene Review

AGO1  -  argonaute RISC catalytic component 1

Homo sapiens

Synonyms: Argonaute RISC catalytic component 1, Argonaute1, EIF2C, EIF2C1, Eukaryotic translation initiation factor 2C 1, ...
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Disease relevance of EIF2C1

  • Anti-Su autoantibodies from both human patients with rheumatic diseases and a mouse model of autoimmunity recognize the endonucleolytic Argonaute and Dicer proteins, both crucial enzymes of the RNAi pathway [1].

High impact information on EIF2C1

  • Argonaute proteins are key players in gene silencing involving small RNAs [2].
  • Hallmarks of small RNAs are their dependence on double-stranded RNAs (dsRNA)-specific RNase III-type enzymes for biogenesis and their association with Argonaute family proteins for the silencing process [3].
  • The Argonaute family: tentacles that reach into RNAi, developmental control, stem cell maintenance, and tumorigenesis [4].
  • Biochemical analysis indicates that AIN-1 interacts with protein complexes containing an Argonaute protein, Dicer, and miRNAs [5].
  • The developmental timing regulator AIN-1 interacts with miRISCs and may target the argonaute protein ALG-1 to cytoplasmic P bodies in C. elegans [5].

Biological context of EIF2C1


Anatomical context of EIF2C1

  • A number of genes have been identified as members of the Argonaute family in various nonhuman organisms and these genes are considered to play important roles in the development and maintenance of germ-line stem cells [7].
  • PCR analysis using human multitissue cDNA panels indicated that all four members of the PIWI subfamily are expressed mainly in the testis, whereas all four members of the eIF2C/AGO subfamily are expressed in a variety of adult tissues [7].
  • To understand the biological function of the different Ago proteins, we set out to determine if Ago1 through Ago4 are associated with miRNAs as well as RISC activity in human cell lines [10].
  • Drosophila Me31B is shown to participate (1) with an FMRP-associated, P body protein (Scd6p/trailer hitch) in FMRP-driven, argonaute-dependent translational repression in developing eye imaginal discs; (2) in dendritic elaboration of larval sensory neurons; and (3) in bantam miRNA-mediated translational repression in wing imaginal discs [11].
  • A fraction of Argonaute proteins and miRNAs biochemically cosediment with polyribosomes, yet another fraction paradoxically accumulates in ribosome-free processing bodies (PBs) in the cytoplasm [12].

Associations of EIF2C1 with chemical compounds


Regulatory relationships of EIF2C1

  • Further investigation revealed that nuclear import of the mitosis-inducing phosphatase Cdc25 is inhibited by overexpression of the Ago1 amino terminus [14].

Other interactions of EIF2C1

  • We postulate that at least some members of the human Argonaute family may be involved in the development and maintenance of stem cells through the RNA-mediated gene-quelling mechanisms associated with DICER [7].
  • Involvement of AGO1 and AGO2 in mammalian transcriptional silencing [15].
  • Particularly, microRNA (miRNA)-mediated translational repression involving PIWI/Argonaute family proteins has been widely recognized as a novel mechanism of gene regulation [16].
  • Here, we show that the Argonaute proteins physically interact with a key P-/GW-body subunit, GW182 [17].

Analytical, diagnostic and therapeutic context of EIF2C1

  • Immunoprecipitation and affinity binding experiments using human HEK293 cells cotransfected with cDNAs for FLAG-tagged DICER, a member of the ribonuclease III family, and the His-tagged members of the Argonaute family suggested that the proteins from members of both subfamilies are associated with DICER [7].
  • Multiple Argonaute sub-families can be identified phylogenetically yet, despite this diversity, molecular and sequence analyses show that Argonaute proteins share common molecular properties and the capacity to function through a common mechanism [18].


  1. The RNA interference pathway: a new target for autoimmunity. Pruijn, G.J. Arthritis Res. Ther. (2006) [Pubmed]
  2. Knocking out the Argonautes. Steiner, F.A., Plasterk, R.H. Cell (2006) [Pubmed]
  3. Small RNAs just got bigger: Piwi-interacting RNAs (piRNAs) in mammalian testes. Kim, V.N. Genes Dev. (2006) [Pubmed]
  4. The Argonaute family: tentacles that reach into RNAi, developmental control, stem cell maintenance, and tumorigenesis. Carmell, M.A., Xuan, Z., Zhang, M.Q., Hannon, G.J. Genes Dev. (2002) [Pubmed]
  5. The developmental timing regulator AIN-1 interacts with miRISCs and may target the argonaute protein ALG-1 to cytoplasmic P bodies in C. elegans. Ding, L., Spencer, A., Morita, K., Han, M. Mol. Cell (2005) [Pubmed]
  6. Human eukaryotic initiation factor EIF2C1 gene: cDNA sequence, genomic organization, localization to chromosomal bands 1p34-p35, and expression. Koesters, R., Adams, V., Betts, D., Moos, R., Schmid, M., Siermann, A., Hassam, S., Weitz, S., Lichter, P., Heitz, P.U., von Knebel Doeberitz, M., Briner, J. Genomics (1999) [Pubmed]
  7. Identification of eight members of the Argonaute family in the human genome small star, filled. Sasaki, T., Shiohama, A., Minoshima, S., Shimizu, N. Genomics (2003) [Pubmed]
  8. Effects of Dicer and Argonaute down-regulation on mRNA levels in human HEK293 cells. Schmitter, D., Filkowski, J., Sewer, A., Pillai, R.S., Oakeley, E.J., Zavolan, M., Svoboda, P., Filipowicz, W. Nucleic Acids Res. (2006) [Pubmed]
  9. MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies. Liu, J., Valencia-Sanchez, M.A., Hannon, G.J., Parker, R. Nat. Cell Biol. (2005) [Pubmed]
  10. Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs. Meister, G., Landthaler, M., Patkaniowska, A., Dorsett, Y., Teng, G., Tuschl, T. Mol. Cell (2004) [Pubmed]
  11. Staufen- and FMRP-Containing Neuronal RNPs Are Structurally and Functionally Related to Somatic P Bodies. Barbee, S.A., Estes, P.S., Cziko, A.M., Hillebrand, J., Luedeman, R.A., Coller, J.M., Johnson, N., Howlett, I.C., Geng, C., Ueda, R., Brand, A.H., Newbury, S.F., Wilhelm, J.E., Levine, R.B., Nakamura, A., Parker, R., Ramaswami, M. Neuron (2006) [Pubmed]
  12. Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules. Leung, A.K., Calabrese, J.M., Sharp, P.A. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  13. Function of the Trypanosome Argonaute 1 protein in RNA interference requires the N-terminal RGG domain and arginine 735 in the Piwi domain. Shi, H., Ullu, E., Tschudi, C. J. Biol. Chem. (2004) [Pubmed]
  14. Interactions between the RNA Interference Effector Protein Ago1 and 14-3-3 Proteins: CONSEQUENCES FOR CELL CYCLE PROGRESSION. Stoica, C., Carmichael, J.B., Parker, H., Pare, J., Hobman, T.C. J. Biol. Chem. (2006) [Pubmed]
  15. Involvement of AGO1 and AGO2 in mammalian transcriptional silencing. Janowski, B.A., Huffman, K.E., Schwartz, J.C., Ram, R., Nordsell, R., Shames, D.S., Minna, J.D., Corey, D.R. Nat. Struct. Mol. Biol. (2006) [Pubmed]
  16. MIWI associates with translational machinery and PIWI-interacting RNAs (piRNAs) in regulating spermatogenesis. Grivna, S.T., Pyhtila, B., Lin, H. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  17. A role for the P-body component GW182 in microRNA function. Liu, J., Rivas, F.V., Wohlschlegel, J., Yates, J.R., Parker, R., Hannon, G.J. Nat. Cell Biol. (2005) [Pubmed]
  18. Argonaute: a scaffold for the function of short regulatory RNAs. Parker, J.S., Barford, D. Trends Biochem. Sci. (2006) [Pubmed]
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